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Solution structure of a zinc domain conserved in yeast copper-regulated transcription factors

Nature Structural Biology volume 5, pages 551–555 (1998)Cite this article

Abstract

The three dimensional structure of the N-terminal domain (residues 1–42) of the copper-responsive transcription factor Amt1 from Candida glabrata has been determined by two-dimensional 1 H-correlated nuclear magnetic resonance (NMR) methods. The domain contains an array of zinc-binding residues (Cys-X 2 -Cys-X 8 -Cys-X-His) that is conserved among a family of Cu-responsive transcription factors. The structure is unlike those of previously characterized zinc finger motifs, and consists of a three-stranded antiparallel ß-sheet with two short helical segments that project from one end of the ß-sheet. Conserved residues at positions 16, 18 and 19 form a basic patch that may be important for DNA binding.

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Figure 1: a, Portion of the 2D NOESY spectrum (200 ms mixing period) obtained for ZnAMT42 showing sequential NH-NH dipolar connectivities.
Figure 2: Summary of sequential (i to i + 1), medium range (i to i + 2–5) and long-range (i to i + >5) NOE connectivities observed in the 2D NOESY spectra of ZnAmt42.
Figure 3: a, Stereo view showing the best-fit superposition of the 15 refined Amt42 zinc domain structures (see Table 1 for statistical information).
Figure 4: Sequence conservation of the 40-residue Zn module in fungal proteins, including Amt1 from Candida Glabrata, Ace1, Mac1 and Lpz8 (YPR008w) from Saccharomyces cerevisiae, Crf1 from Yarrowia lipolytica (accession number Z23265), Ac31 from Schizosaccharomyces pombe (C31A2.11c, chromosome I), and Grisea from Podospora anserina.

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Acknowledgements

Support from the National Institutes of Health (to D.R.W, M.C.P. and the Biotechnology Core Facility at the University of Utah), and technical assistance from R. Edwards (HHMI-UMBC) is gratefully acknowledged. R.B.T. and D.L.S. are Meyerhoff Undergraduate Scholars at UMBC.

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Author notes

  1. Ryan B. Turner and Danielle L. Smith: These authors contributed equally to the structure determination.

Authors and Affiliations

  1. Howard Hughes Medical Institute and Department of Chemistry and Biochemistry, University of Maryland Baltimore County, Baltimore, 21250, Maryland, USA

    Ryan B. Turner, Danielle L. Smith, Michael E. Zawrotny & Michael F. Summers

  2. University of Utah Health Sciences Center, Salt Lake City, 84132, Utah, USA

    Matthew C. Posewitz & Dennis R. Winge

Authors
  1. Ryan B. Turner
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  2. Danielle L. Smith
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Correspondence to Michael F. Summers or Dennis R. Winge.

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Turner, R., Smith, D., Zawrotny, M. et al. Solution structure of a zinc domain conserved in yeast copper-regulated transcription factors. Nat Struct Mol Biol 5, 551–555 (1998). https://doi.org/10.1038/805

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